Lea Dietrich, Ahmed-Noor A. Agip, Christina Kunz, Andre Schwarz, Werner Kühlbrandt
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引用次数: 0
摘要
细胞依赖于三磷酸腺苷(ATP)这种通用能源货币的持续供应。在线粒体中,ATP 通过一系列氧化还原反应产生,在线粒体内膜上形成电化学梯度。ATP 合成酶利用梯度的能量,从二磷酸腺苷(ADP)和无机磷酸生成 ATP。我们通过电子低温断层扫描和子图平均法,以高达4.2埃的分辨率测定了单细胞鞭毛虫多角体线粒体内ATP合成酶的结构,揭示了中央柄的六个旋转位置,细分为F1头的21个亚态。多瘤病毒的 ATP 合酶形成螺旋阵列,多个相邻行定义了嵴脊。在膜电位存在的原生工作条件下的 ATP 合成酶结构是原位分析膜蛋白复合物的关键一步。
In situ structure and rotary states of mitochondrial ATP synthase in whole Polytomella cells
Cells depend on a continuous supply of adenosine triphosphate (ATP), the universal energy currency. In mitochondria, ATP is produced by a series of redox reactions, whereby an electrochemical gradient is established across the inner mitochondrial membrane. The ATP synthase harnesses the energy of the gradient to generate ATP from adenosine diphosphate (ADP) and inorganic phosphate. We determined the structure of ATP synthase within mitochondria of the unicellular flagellate Polytomella by electron cryo-tomography and subtomogram averaging at up to 4.2-angstrom resolution, revealing six rotary positions of the central stalk, subclassified into 21 substates of the F1 head. The Polytomella ATP synthase forms helical arrays with multiple adjacent rows defining the cristae ridges. The structure of ATP synthase under native operating conditions in the presence of a membrane potential represents a pivotal step toward the analysis of membrane protein complexes in situ.
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